|
Name |
Accession |
Description |
Interval |
E-value |
| gyrB |
PRK14939 |
DNA gyrase subunit B; Provisional |
1-339 |
0e+00 |
|
DNA gyrase subunit B; Provisional
Pssm-ID: 237860 [Multi-domain] Cd Length: 756 Bit Score: 691.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 1 LLLTIRRNGHVYEQTYHLGEPQAPLKQIGDSSsGTGTEVRFWPSSTIFSDTLFHYDILAKRLRELSFLNSGVSIRLEDER 80
Cdd:PRK14939 132 LELTIRRDGKIHEQEFEHGVPVAPLKVVGETD-KTGTEVRFWPSPEIFENTEFDYDILAKRLRELAFLNSGVRIRLKDER 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 81 DGREVHFCYEGGIKAFVEYLNQNKTPIHPKVFHFTTEQDGIGVEVAMQWNDAYQEGVYCFTNNIPQRDGGTHLVGFRTAL 160
Cdd:PRK14939 211 DGKEEEFHYEGGIKAFVEYLNRNKTPLHPNIFYFSGEKDGIGVEVALQWNDSYQENVLCFTNNIPQRDGGTHLAGFRAAL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 161 TRTLNTYMDKEDYSKKAK*SAAsGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKLGEFLLENPGDA 240
Cdd:PRK14939 291 TRTINNYIEKEGLAKKAKVSLT-GDDAREGLTAVLSVKVPDPKFSSQTKDKLVSSEVRPAVESLVNEKLSEFLEENPNEA 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 241 KIVVNKIIDAARAREAARKARELTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAKQGRNRKNQAILPLKG 320
Cdd:PRK14939 370 KIIVGKIIDAARAREAARKARELTRRKGALDIAGLPGKLADCQEKDPALSELYLVEGDSAGGSAKQGRDRKFQAILPLKG 449
|
330
....*....|....*....
gi 1173202403 321 KILNVEKARFDKMISSQEV 339
Cdd:PRK14939 450 KILNVEKARFDKMLSSQEI 468
|
|
| GyrB |
COG0187 |
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair]; |
1-339 |
0e+00 |
|
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair];
Pssm-ID: 439957 [Multi-domain] Cd Length: 635 Bit Score: 533.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 1 LLLTIRRNGHVYEQTYHLGEPQAPLKQIGDSSsGTGTEVRFWPSSTIFSDTLFHYDILAKRLRELSFLNSGVSIRLEDER 80
Cdd:COG0187 130 LEVEVKRDGKIYRQRFERGKPVGPLEKIGKTD-RTGTTVRFKPDPEIFETTEFDYETLAERLRELAFLNKGLTITLTDER 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 81 DG--REVHFCYEGGIKAFVEYLNQNKTPIHPKVFHFTTEQDGIGVEVAMQWNDAYQEGVYCFTNNIPQRDGGTHLVGFRT 158
Cdd:COG0187 209 EEepKEETFHYEGGIKDFVEYLNEDKEPLHPEVIYFEGEKDGIEVEVALQWNDGYSENIHSFVNNINTPEGGTHETGFRT 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 159 ALTRTLNTYMDKEDySKKAK*SAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKLGEFLLENPG 238
Cdd:COG0187 289 ALTRVINDYARKNG-LLKEKDKNLTGDDVREGLTAVISVKLPEPQFEGQTKTKLGNSEARGIVESVVSEKLEHYLEENPA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 239 DAKIVVNKIIDAARAREAARKARELTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAKQGRNRKNQAILPL 318
Cdd:COG0187 368 EAKKILEKAILAARAREAARKARELVRRKSALESSGLPGKLADCSSKDPEESELFIVEGDSAGGSAKQGRDREFQAILPL 447
|
330 340
....*....|....*....|.
gi 1173202403 319 KGKILNVEKARFDKMISSQEV 339
Cdd:COG0187 448 RGKILNVEKARLDKILKNEEI 468
|
|
| gyrB |
TIGR01059 |
DNA gyrase, B subunit; This model describes the common type II DNA topoisomerase (DNA gyrase). ... |
1-339 |
0e+00 |
|
DNA gyrase, B subunit; This model describes the common type II DNA topoisomerase (DNA gyrase). Two apparently independently arising families, one in the Proteobacteria and one in Gram-positive lineages, are both designated toposisomerase IV. Proteins scoring above the noise cutoff for this model and below the trusted cutoff for topoisomerase IV models probably should be designated GyrB. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273421 [Multi-domain] Cd Length: 654 Bit Score: 533.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 1 LLLTIRRNGHVYEQTYHLGEPQAPLKQIGDSSSgTGTEVRFWPSSTIFSDTLFHYDILAKRLRELSFLNSGVSIRLEDER 80
Cdd:TIGR01059 125 LEVTVFRDGKIYRQEFERGIPVGPLEVVGETKK-TGTTVRFWPDPEIFETTEFDFDILAKRLRELAFLNSGVKISLEDER 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 81 D--GREVHFCYEGGIKAFVEYLNQNKTPIHPKVFHFTTEQDGIGVEVAMQWNDAYQEGVYCFTNNIPQRDGGTHLVGFRT 158
Cdd:TIGR01059 204 DgkGKKVTFHYEGGIKSFVKYLNRNKEPLHEEIIYIKGEKEGIEVEVALQWNDGYSENILSFVNNINTREGGTHLEGFRS 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 159 ALTRTLNTYMDKEDYsKKAK*SAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKLGEFLLENPG 238
Cdd:TIGR01059 284 ALTRVINSYAKNNKL-LKESKPNLTGEDIREGLTAVISVKVPDPQFEGQTKTKLGNSEVRSIVESLVYEKLTEFFEENPQ 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 239 DAKIVVNKIIDAARAREAARKARELTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAKQGRNRKNQAILPL 318
Cdd:TIGR01059 363 EAKAIVEKAILAAQAREAARKARELTRRKSALDSGGLPGKLADCSSKDPSKSELYIVEGDSAGGSAKQGRDRRFQAILPL 442
|
330 340
....*....|....*....|.
gi 1173202403 319 KGKILNVEKARFDKMISSQEV 339
Cdd:TIGR01059 443 RGKILNVEKARLDKILSNQEI 463
|
|
| TOP2c |
smart00433 |
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE |
1-339 |
9.50e-136 |
|
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE
Pssm-ID: 214659 [Multi-domain] Cd Length: 594 Bit Score: 398.47 E-value: 9.50e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 1 LLLTIRRNGHVYEQTYH-LGEPQAPLKQIGDSSSgTGTEVRFWPSSTIFS-DTLFHYDILAKRLRELSFLNSGVSIRLED 78
Cdd:smart00433 96 FEVEVARDGKEYKQSFSnNGKPLSEPKIIGDTKK-DGTKVTFKPDLEIFGmTTDDDFELLKRRLRELAFLNKGVKITLND 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 79 ERDGREVHFCYEGGIKAFVEYLNQNKTPIHPKVFHFTTEQDGIGVEVAMQWNDAYQEGVYCFTNNIPQRDGGTHLVGFRT 158
Cdd:smart00433 175 ERSDEEKTFLFEGGIKDYVELLNKNKELLSPEPTYIEGEKDNIRVEVAFQYTDGYSENIVSFVNNIATTEGGTHENGFKD 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 159 ALTRTLNTYMDKedySKKAK*SAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKLGEFLLENPG 238
Cdd:smart00433 255 ALTRVINEYAKK---KKKLKEKNIKGEDVREGLTAFISVKIPEPQFEGQTKEKLGTSEVRFGVEKIVSECLLSFLEENPV 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 239 DAKIVVNKIIDAARAREAARKARELTRRKgALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAKQGRNRKNQAILPL 318
Cdd:smart00433 332 EASKIVEKVLLAAKARAAAKKARELTRKK-KLSSISLPGKLADASSAGPKKCELFLVEGDSAGGSAKSGRDRDFQAILPL 410
|
330 340
....*....|....*....|.
gi 1173202403 319 KGKILNVEKARFDKMISSQEV 339
Cdd:smart00433 411 RGKILNVEKASLDKILKNEEI 431
|
|
| TopoII_Trans_DNA_gyrase |
cd00822 |
TopoIIA_Trans_DNA_gyrase: Transducer domain, having a ribosomal S5 domain 2-like fold, of the ... |
91-249 |
1.34e-78 |
|
TopoIIA_Trans_DNA_gyrase: Transducer domain, having a ribosomal S5 domain 2-like fold, of the type found in proteins of the type IIA family of DNA topoisomerases similar to the B subunits of E. coli DNA gyrase and E. coli Topoisomerase IV which are heterodimers composed of two subunits. The type IIA enzymes are the predominant form of topoisomerase and are found in some bacteriophages, viruses and archaea, and in all bacteria and eukaryotes. All type IIA topoisomerases are related to each other at amino acid sequence level, though their oligomeric organization sometimes differs. TopoIIA enzymes cut both strands of the duplex DNA to remove (relax) both positive and negative supercoils in DNA. These enzymes covalently attach to the 5' ends of the cut DNA, separate the free ends of the cleaved strands, pass another region of the duplex through this gap, then rejoin the ends. TopoIIA enzymes also catenate/ decatenate duplex rings. E.coli DNA gyrase is a heterodimer composed of two subunits. E. coli DNA gyrase B subunit is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes.
Pssm-ID: 238419 [Multi-domain] Cd Length: 172 Bit Score: 237.84 E-value: 1.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 91 GGIKAFVEYLNQNKTPIHPKVFHFTTEQDGIGVEVAMQWNDAYQEGVYCFTNNIPQRDGGTHLVGFRTALTRTLNTYMDK 170
Cdd:cd00822 1 GGLKDFVEELNKDKEPLHEEPIYIEGEKDGVEVEVALQWTDSYSENILSFVNNIPTPEGGTHETGFRAALTRAINDYAKK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1173202403 171 EDYsKKAK*SAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKLGEFLLENPGDAKIVVNKIID 249
Cdd:cd00822 81 NNL-LKKKDVKLTGDDIREGLTAVISVKVPEPQFEGQTKDKLGNSEVRSIVESAVREALEEWLEENPEEAKKILEKAIL 158
|
|
| DNA_gyraseB |
pfam00204 |
DNA gyrase B; This family represents the second domain of DNA gyrase B which has a ribosomal ... |
92-249 |
2.35e-65 |
|
DNA gyrase B; This family represents the second domain of DNA gyrase B which has a ribosomal S5 domain 2-like fold. This family is structurally related to PF01119.
Pssm-ID: 425522 [Multi-domain] Cd Length: 173 Bit Score: 204.00 E-value: 2.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 92 GIKAFVEYLNQNKTPIHPKVFHFTTE--QDGIGVEVAMQWNDAYQEGVYCFTNNIPQRDGGTHLVGFRTALTRTLNTYMD 169
Cdd:pfam00204 1 GLKDFVEELNKDKKPLHKEIIYFEGEspDNRIEVEVALQWTDSYSENILSFVNNIATPEGGTHVDGFKSALTRTINEYAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 170 KEDYSKKAK*SAAsGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKLGEFLLENPGDAKIVVNKIID 249
Cdd:pfam00204 81 KKGLLKKKDEKIT-GEDIREGLTAVVSVKIPDPQFEGQTKEKLGNPEVKSAVEKIVSEKLEEFLEENPEIAKKILEKALQ 159
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| gyrB |
PRK14939 |
DNA gyrase subunit B; Provisional |
1-339 |
0e+00 |
|
DNA gyrase subunit B; Provisional
Pssm-ID: 237860 [Multi-domain] Cd Length: 756 Bit Score: 691.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 1 LLLTIRRNGHVYEQTYHLGEPQAPLKQIGDSSsGTGTEVRFWPSSTIFSDTLFHYDILAKRLRELSFLNSGVSIRLEDER 80
Cdd:PRK14939 132 LELTIRRDGKIHEQEFEHGVPVAPLKVVGETD-KTGTEVRFWPSPEIFENTEFDYDILAKRLRELAFLNSGVRIRLKDER 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 81 DGREVHFCYEGGIKAFVEYLNQNKTPIHPKVFHFTTEQDGIGVEVAMQWNDAYQEGVYCFTNNIPQRDGGTHLVGFRTAL 160
Cdd:PRK14939 211 DGKEEEFHYEGGIKAFVEYLNRNKTPLHPNIFYFSGEKDGIGVEVALQWNDSYQENVLCFTNNIPQRDGGTHLAGFRAAL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 161 TRTLNTYMDKEDYSKKAK*SAAsGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKLGEFLLENPGDA 240
Cdd:PRK14939 291 TRTINNYIEKEGLAKKAKVSLT-GDDAREGLTAVLSVKVPDPKFSSQTKDKLVSSEVRPAVESLVNEKLSEFLEENPNEA 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 241 KIVVNKIIDAARAREAARKARELTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAKQGRNRKNQAILPLKG 320
Cdd:PRK14939 370 KIIVGKIIDAARAREAARKARELTRRKGALDIAGLPGKLADCQEKDPALSELYLVEGDSAGGSAKQGRDRKFQAILPLKG 449
|
330
....*....|....*....
gi 1173202403 321 KILNVEKARFDKMISSQEV 339
Cdd:PRK14939 450 KILNVEKARFDKMLSSQEI 468
|
|
| gyrB |
PRK05644 |
DNA gyrase subunit B; Validated |
4-339 |
0e+00 |
|
DNA gyrase subunit B; Validated
Pssm-ID: 235542 [Multi-domain] Cd Length: 638 Bit Score: 533.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 4 TIRRNGHVYEQTYHLGEPQAPLKQIGDSSsGTGTEVRFWPSSTIFSDTLFHYDILAKRLRELSFLNSGVSIRLEDERDG- 82
Cdd:PRK05644 135 EVKRDGKIYYQEYERGVPVTPLEVIGETD-ETGTTVTFKPDPEIFETTEFDYDTLATRLRELAFLNKGLKITLTDEREGe 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 83 -REVHFCYEGGIKAFVEYLNQNKTPIHPKVFHFTTEQDGIGVEVAMQWNDAYQEGVYCFTNNIPQRDGGTHLVGFRTALT 161
Cdd:PRK05644 214 eKEETFHYEGGIKEYVEYLNRNKEPLHEEPIYFEGEKDGIEVEVAMQYNDGYSENILSFANNINTHEGGTHEEGFKTALT 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 162 RTLNTYMDKEDYSKKAK*SAAsGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKLGEFLLENPGDAK 241
Cdd:PRK05644 294 RVINDYARKNKLLKEKDDNLT-GEDVREGLTAVISVKHPEPQFEGQTKTKLGNSEVRGIVDSVVSEALSEFLEENPNVAK 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 242 IVVNKIIDAARAREAARKARELTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAKQGRNRKNQAILPLKGK 321
Cdd:PRK05644 373 KIVEKAILAARAREAARKARELTRRKSALESSSLPGKLADCSSKDPEESELYIVEGDSAGGSAKQGRDRRFQAILPLRGK 452
|
330
....*....|....*...
gi 1173202403 322 ILNVEKARFDKMISSQEV 339
Cdd:PRK05644 453 ILNVEKARLDKILKNEEI 470
|
|
| GyrB |
COG0187 |
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair]; |
1-339 |
0e+00 |
|
DNA gyrase/topoisomerase IV, subunit B [Replication, recombination and repair];
Pssm-ID: 439957 [Multi-domain] Cd Length: 635 Bit Score: 533.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 1 LLLTIRRNGHVYEQTYHLGEPQAPLKQIGDSSsGTGTEVRFWPSSTIFSDTLFHYDILAKRLRELSFLNSGVSIRLEDER 80
Cdd:COG0187 130 LEVEVKRDGKIYRQRFERGKPVGPLEKIGKTD-RTGTTVRFKPDPEIFETTEFDYETLAERLRELAFLNKGLTITLTDER 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 81 DG--REVHFCYEGGIKAFVEYLNQNKTPIHPKVFHFTTEQDGIGVEVAMQWNDAYQEGVYCFTNNIPQRDGGTHLVGFRT 158
Cdd:COG0187 209 EEepKEETFHYEGGIKDFVEYLNEDKEPLHPEVIYFEGEKDGIEVEVALQWNDGYSENIHSFVNNINTPEGGTHETGFRT 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 159 ALTRTLNTYMDKEDySKKAK*SAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKLGEFLLENPG 238
Cdd:COG0187 289 ALTRVINDYARKNG-LLKEKDKNLTGDDVREGLTAVISVKLPEPQFEGQTKTKLGNSEARGIVESVVSEKLEHYLEENPA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 239 DAKIVVNKIIDAARAREAARKARELTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAKQGRNRKNQAILPL 318
Cdd:COG0187 368 EAKKILEKAILAARAREAARKARELVRRKSALESSGLPGKLADCSSKDPEESELFIVEGDSAGGSAKQGRDREFQAILPL 447
|
330 340
....*....|....*....|.
gi 1173202403 319 KGKILNVEKARFDKMISSQEV 339
Cdd:COG0187 448 RGKILNVEKARLDKILKNEEI 468
|
|
| gyrB |
TIGR01059 |
DNA gyrase, B subunit; This model describes the common type II DNA topoisomerase (DNA gyrase). ... |
1-339 |
0e+00 |
|
DNA gyrase, B subunit; This model describes the common type II DNA topoisomerase (DNA gyrase). Two apparently independently arising families, one in the Proteobacteria and one in Gram-positive lineages, are both designated toposisomerase IV. Proteins scoring above the noise cutoff for this model and below the trusted cutoff for topoisomerase IV models probably should be designated GyrB. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273421 [Multi-domain] Cd Length: 654 Bit Score: 533.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 1 LLLTIRRNGHVYEQTYHLGEPQAPLKQIGDSSSgTGTEVRFWPSSTIFSDTLFHYDILAKRLRELSFLNSGVSIRLEDER 80
Cdd:TIGR01059 125 LEVTVFRDGKIYRQEFERGIPVGPLEVVGETKK-TGTTVRFWPDPEIFETTEFDFDILAKRLRELAFLNSGVKISLEDER 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 81 D--GREVHFCYEGGIKAFVEYLNQNKTPIHPKVFHFTTEQDGIGVEVAMQWNDAYQEGVYCFTNNIPQRDGGTHLVGFRT 158
Cdd:TIGR01059 204 DgkGKKVTFHYEGGIKSFVKYLNRNKEPLHEEIIYIKGEKEGIEVEVALQWNDGYSENILSFVNNINTREGGTHLEGFRS 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 159 ALTRTLNTYMDKEDYsKKAK*SAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKLGEFLLENPG 238
Cdd:TIGR01059 284 ALTRVINSYAKNNKL-LKESKPNLTGEDIREGLTAVISVKVPDPQFEGQTKTKLGNSEVRSIVESLVYEKLTEFFEENPQ 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 239 DAKIVVNKIIDAARAREAARKARELTRRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAKQGRNRKNQAILPL 318
Cdd:TIGR01059 363 EAKAIVEKAILAAQAREAARKARELTRRKSALDSGGLPGKLADCSSKDPSKSELYIVEGDSAGGSAKQGRDRRFQAILPL 442
|
330 340
....*....|....*....|.
gi 1173202403 319 KGKILNVEKARFDKMISSQEV 339
Cdd:TIGR01059 443 RGKILNVEKARLDKILSNQEI 463
|
|
| TOP2c |
smart00433 |
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE |
1-339 |
9.50e-136 |
|
TopoisomeraseII; Eukaryotic DNA topoisomerase II, GyrB, ParE
Pssm-ID: 214659 [Multi-domain] Cd Length: 594 Bit Score: 398.47 E-value: 9.50e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 1 LLLTIRRNGHVYEQTYH-LGEPQAPLKQIGDSSSgTGTEVRFWPSSTIFS-DTLFHYDILAKRLRELSFLNSGVSIRLED 78
Cdd:smart00433 96 FEVEVARDGKEYKQSFSnNGKPLSEPKIIGDTKK-DGTKVTFKPDLEIFGmTTDDDFELLKRRLRELAFLNKGVKITLND 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 79 ERDGREVHFCYEGGIKAFVEYLNQNKTPIHPKVFHFTTEQDGIGVEVAMQWNDAYQEGVYCFTNNIPQRDGGTHLVGFRT 158
Cdd:smart00433 175 ERSDEEKTFLFEGGIKDYVELLNKNKELLSPEPTYIEGEKDNIRVEVAFQYTDGYSENIVSFVNNIATTEGGTHENGFKD 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 159 ALTRTLNTYMDKedySKKAK*SAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKLGEFLLENPG 238
Cdd:smart00433 255 ALTRVINEYAKK---KKKLKEKNIKGEDVREGLTAFISVKIPEPQFEGQTKEKLGTSEVRFGVEKIVSECLLSFLEENPV 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 239 DAKIVVNKIIDAARAREAARKARELTRRKgALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAKQGRNRKNQAILPL 318
Cdd:smart00433 332 EASKIVEKVLLAAKARAAAKKARELTRKK-KLSSISLPGKLADASSAGPKKCELFLVEGDSAGGSAKSGRDRDFQAILPL 410
|
330 340
....*....|....*....|.
gi 1173202403 319 KGKILNVEKARFDKMISSQEV 339
Cdd:smart00433 411 RGKILNVEKASLDKILKNEEI 431
|
|
| PRK05559 |
PRK05559 |
DNA topoisomerase IV subunit B; Reviewed |
4-339 |
4.56e-133 |
|
DNA topoisomerase IV subunit B; Reviewed
Pssm-ID: 235501 [Multi-domain] Cd Length: 631 Bit Score: 392.54 E-value: 4.56e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 4 TIRRNGHVYEQTYHLGEPQAPLKQIGDSSSG-TGTEVRFWPSSTIFSDTLFHYDILAKRLRELSFLNSGVSIRLEDERDG 82
Cdd:PRK05559 135 EVKRDGKVYRQRFEGGDPVGPLEVVGTAGKRkTGTRVRFWPDPKIFDSPKFSPERLKERLRSKAFLLPGLTITLNDERER 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 83 REvhFCYEGGIKAFVEYLNQNKTPIHP-KVFHFTTEQDGIGVEVAMQWNDAYQEGVYCFTNNIPQRDGGTHLVGFRTALT 161
Cdd:PRK05559 215 QT--FHYENGLKDYLAELNEGKETLPEeFVGSFEGEAEGEAVEWALQWTDEGGENIESYVNLIPTPQGGTHENGFREGLL 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 162 RTLNTYMDKedYSKKAK*SAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKLGEFLLENPGDAK 241
Cdd:PRK05559 293 KAVREFAEK--RNLLPKGKKLEGEDVREGLAAVLSVKIPEPQFEGQTKEKLGSREARRFVSGVVKDAFDLWLNQNPELAE 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 242 IVVNKIIDAARAREAARKARelTRRKGALDIAgLPGKLADCQEKDPALSELYIVEGDSAGGSAKQGRNRKNQAILPLKGK 321
Cdd:PRK05559 371 KLAEKAIKAAQARLRAAKKV--KRKKKTSGPA-LPGKLADCTSQDPERTELFLVEGDSAGGSAKQARDREFQAILPLRGK 447
|
330
....*....|....*...
gi 1173202403 322 ILNVEKARFDKMISSQEV 339
Cdd:PRK05559 448 ILNTWEASLDDVLANEEI 465
|
|
| TopoII_Trans_DNA_gyrase |
cd00822 |
TopoIIA_Trans_DNA_gyrase: Transducer domain, having a ribosomal S5 domain 2-like fold, of the ... |
91-249 |
1.34e-78 |
|
TopoIIA_Trans_DNA_gyrase: Transducer domain, having a ribosomal S5 domain 2-like fold, of the type found in proteins of the type IIA family of DNA topoisomerases similar to the B subunits of E. coli DNA gyrase and E. coli Topoisomerase IV which are heterodimers composed of two subunits. The type IIA enzymes are the predominant form of topoisomerase and are found in some bacteriophages, viruses and archaea, and in all bacteria and eukaryotes. All type IIA topoisomerases are related to each other at amino acid sequence level, though their oligomeric organization sometimes differs. TopoIIA enzymes cut both strands of the duplex DNA to remove (relax) both positive and negative supercoils in DNA. These enzymes covalently attach to the 5' ends of the cut DNA, separate the free ends of the cleaved strands, pass another region of the duplex through this gap, then rejoin the ends. TopoIIA enzymes also catenate/ decatenate duplex rings. E.coli DNA gyrase is a heterodimer composed of two subunits. E. coli DNA gyrase B subunit is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes.
Pssm-ID: 238419 [Multi-domain] Cd Length: 172 Bit Score: 237.84 E-value: 1.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 91 GGIKAFVEYLNQNKTPIHPKVFHFTTEQDGIGVEVAMQWNDAYQEGVYCFTNNIPQRDGGTHLVGFRTALTRTLNTYMDK 170
Cdd:cd00822 1 GGLKDFVEELNKDKEPLHEEPIYIEGEKDGVEVEVALQWTDSYSENILSFVNNIPTPEGGTHETGFRAALTRAINDYAKK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1173202403 171 EDYsKKAK*SAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKLGEFLLENPGDAKIVVNKIID 249
Cdd:cd00822 81 NNL-LKKKDVKLTGDDIREGLTAVISVKVPEPQFEGQTKDKLGNSEVRSIVESAVREALEEWLEENPEEAKKILEKAIL 158
|
|
| DNA_gyraseB |
pfam00204 |
DNA gyrase B; This family represents the second domain of DNA gyrase B which has a ribosomal ... |
92-249 |
2.35e-65 |
|
DNA gyrase B; This family represents the second domain of DNA gyrase B which has a ribosomal S5 domain 2-like fold. This family is structurally related to PF01119.
Pssm-ID: 425522 [Multi-domain] Cd Length: 173 Bit Score: 204.00 E-value: 2.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 92 GIKAFVEYLNQNKTPIHPKVFHFTTE--QDGIGVEVAMQWNDAYQEGVYCFTNNIPQRDGGTHLVGFRTALTRTLNTYMD 169
Cdd:pfam00204 1 GLKDFVEELNKDKKPLHKEIIYFEGEspDNRIEVEVALQWTDSYSENILSFVNNIATPEGGTHVDGFKSALTRTINEYAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 170 KEDYSKKAK*SAAsGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKLGEFLLENPGDAKIVVNKIID 249
Cdd:pfam00204 81 KKGLLKKKDEKIT-GEDIREGLTAVVSVKIPDPQFEGQTKEKLGNPEVKSAVEKIVSEKLEEFLEENPEIAKKILEKALQ 159
|
|
| PTZ00109 |
PTZ00109 |
DNA gyrase subunit b; Provisional |
7-334 |
4.02e-62 |
|
DNA gyrase subunit b; Provisional
Pssm-ID: 240272 [Multi-domain] Cd Length: 903 Bit Score: 212.82 E-value: 4.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 7 RNGHVYEQTYHLGEPQAPLKQIGDSSSGTGTEVRFWPS-STIFSDTLFHY--------------DILAKRLRELSFLNSG 71
Cdd:PTZ00109 270 KGGKIYSIELSKGKVTKPLSVFSCPLKKRGTTIHFLPDyKHIFKTHHQHTeteeeegckngfnlDLIKNRIHELSYLNPG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 72 VSIRLEDERDGREVHFC------YEGGIKAFVEYLNQNKTPIHP--KVFHFTTEQDGIGVEVAMQWN-DAYQEGVYCFTN 142
Cdd:PTZ00109 350 LTFYLVDERIANENNFYpyetikHEGGTREFLEELIKDKTPLYKdiNIISIRGVIKNVNVEVSLSWSlESYTALIKSFAN 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 143 NIpQRDGGTHLVGFRTALTRTLNTYMDKEDYSKKAK*SAAsGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVE 222
Cdd:PTZ00109 430 NV-STTAGTHIDGFKYAITRCVNGNIKKNGYFKGNFVNIP-GEFIREGMTAIISVKLNGAEFDGQTKTKLGNHLLKTILE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 223 QAMGEKLGEFLLENPGDAKIVVNKIIDAARAREAARKARELTRRKGALDIA-GLPGKLADCQEKDPALSELYIVEGDSAG 301
Cdd:PTZ00109 508 SIVFEQLSEILEFEPNLLLAIYNKSLAAKKAFEEAKAAKDLIRQKNNQYYStILPGKLVDCISDDIERNELFIVEGESAA 587
|
330 340 350
....*....|....*....|....*....|...
gi 1173202403 302 GSAKQGRNRKNQAILPLKGKILNVEKARFDKMI 334
Cdd:PTZ00109 588 GNAKQARNREFQAVLPLKGKILNIEKIKNNKKV 620
|
|
| parE_Gneg |
TIGR01055 |
DNA topoisomerase IV, B subunit, proteobacterial; Operationally, topoisomerase IV is a type II ... |
3-339 |
9.99e-59 |
|
DNA topoisomerase IV, B subunit, proteobacterial; Operationally, topoisomerase IV is a type II topoisomerase required for the decatenation of chromosome segregation. Not every bacterium has both a topo II and a topo IV. The topo IV families of the Gram-positive bacteria and the Gram-negative bacteria appear not to represent a single clade among the type II topoisomerases, and are represented by separate models for this reason. This protein is active as an alpha(2)beta(2) heterotetramer. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 130127 [Multi-domain] Cd Length: 625 Bit Score: 199.76 E-value: 9.99e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 3 LTIRRNGHVYEQTYHLGEPQAPLKQIGDSSS-GTGTEVRFWPSSTIFSDTLFHYDILAKRLRELSFLNSGVSIRLEDERD 81
Cdd:TIGR01055 127 IKVYRQGKLYSIAFENGAKVTDLISAGTCGKrLTGTSVHFTPDPEIFDSLHFSVSRLYHILRAKAVLCRGVEIEFEDEVN 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 82 GREVHFCYEGGIKAFV-EYLNQNKTPIhPKVFHFTTEQDGIGVEVAMQWNDAYQEGV---YCftNNIPQRDGGTHLVGFR 157
Cdd:TIGR01055 207 NTKALWNYPDGLKDYLsEAVNGDNTLP-PKPFSGNFEGDDEAVEWALLWLPEGGELFmesYV--NLIPTPQGGTHVNGLR 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 158 TALTRTLNTYMdkEDYSKKAK*SAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKLGEFLLENP 237
Cdd:TIGR01055 284 QGLLDALREFC--EMRNNLPRGVKLTAEDIWDRCSYVLSIKMQDPQFAGQTKERLSSRQVAKFVSGVIKDAFDLWLNQNV 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 238 GDAKIVVNKIIDAARAREAARKAREltrRKGALDIAGLPGKLADCQEKDPALSELYIVEGDSAGGSAKQGRNRKNQAILP 317
Cdd:TIGR01055 362 QLAEHLAEHAISSAQRRKRAAKKVV---RKKLTSGPALPGKLADCTRQDLEGTELFLVEGDSAGGSAKQARDREYQAILP 438
|
330 340
....*....|....*....|..
gi 1173202403 318 LKGKILNVEKARFDKMISSQEV 339
Cdd:TIGR01055 439 LWGKILNTWEVSLDKVLNSQEI 460
|
|
| HATPase_GyrB-like |
cd16928 |
Histidine kinase-like ATPase domain of the B subunit of DNA gyrase; This family includes ... |
1-87 |
3.14e-33 |
|
Histidine kinase-like ATPase domain of the B subunit of DNA gyrase; This family includes histidine kinase-like ATPase domain of the B subunit of DNA gyrase. Bacterial DNA gyrase is a type II topoisomerase (type II as it transiently cleaves both strands of DNA) which catalyzes the introduction of negative supercoils into DNA, possibly by a mechanism in which one segment of the double-stranded DNA substrate is passed through a transient break in a second segment. It consists of GyrA and GyrB subunits in an A2B2 stoichiometry; GyrA subunits catalyze strand-breakage and reunion reactions, and GyrB subunits hydrolyze ATP. DNA gyrase is found in bacteria, plants and archaea, but as it is absent in humans it is a possible drug target for the treatment of bacterial and parasite infections.
Pssm-ID: 340405 [Multi-domain] Cd Length: 180 Bit Score: 121.10 E-value: 3.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 1 LLLTIRRNGHVYEQTYHLGEPQAPLKQIGDSSSgTGTEVRFWPSSTIFSDTLFHYDILAKRLRELSFLNSGVSIRLEDER 80
Cdd:cd16928 95 LEVEVKRDGKIYRQEFSRGGPLTPLEVIGETKK-TGTTVRFWPDPEIFEKTEFDFDTLKRRLRELAFLNKGLKIVLEDER 173
|
....*..
gi 1173202403 81 DGREVHF 87
Cdd:cd16928 174 TGKEEVF 180
|
|
| TopoII_MutL_Trans |
cd00329 |
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the ... |
93-212 |
1.92e-22 |
|
MutL_Trans: transducer domain, having a ribosomal S5 domain 2-like fold, conserved in the C-terminal domain of type II DNA topoisomerases (Topo II) and DNA mismatch repair (MutL/MLH1/PMS2) proteins. This transducer domain is homologous to the second domain of the DNA gyrase B subunit, which is known to be important in nucleotide hydrolysis and the transduction of structural signals from ATP-binding site to the DNA breakage/reunion regions of the enzymes. The GyrB dimerizes in response to ATP binding, and is homologous to the N-terminal half of eukaryotic Topo II and the ATPase fragment of MutL. Type II DNA topoisomerases catalyze the ATP-dependent transport of one DNA duplex through another, in the process generating transient double strand breaks via covalent attachments to both DNA strands at the 5' positions. Included in this group are proteins similar to human MLH1 and PMS2. MLH1 forms a heterodimer with PMS2 which functions in meiosis and in DNA mismatch repair (MMR). Cells lacking either hMLH1 or hPMS2 have a strong mutator phenotype and display microsatellite instability (MSI). Mutation in hMLH1 accounts for a large fraction of Lynch syndrome (HNPCC) families.
Pssm-ID: 238202 [Multi-domain] Cd Length: 107 Bit Score: 90.40 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 93 IKAFVEYLNQNKTpiHPKVFHFTTEQDGIGVEVAMQWND---AYQEGVYCFTNNIPQRDGGTHLVGFRTALTRTLNtymd 169
Cdd:cd00329 1 LKDRLAEILGDKV--ADKLIYVEGESDGFRVEGAISYPDsgrSSKDRQFSFVNGRPVREGGTHVKAVREAYTRALN---- 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1173202403 170 kedyskkak*saasGDDVREGLIAVISVKVPD--PKFS-SQTKDKL 212
Cdd:cd00329 75 --------------GDDVRRYPVAVLSLKIPPslVDVNvHPTKEEV 106
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
7-339 |
3.97e-13 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 70.46 E-value: 3.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 7 RNGHVYEQTY--HLGEPQAPlkQIGDSSSGTG-TEVRFWPSSTIFSDTLF---HYDILAKRLRELSFLNSGVSIRLEDER 80
Cdd:PTZ00108 165 KSGKKFKMTWtdNMSKKSEP--RITSYDGKKDyTKVTFYPDYAKFGMTEFdddMLRLLKKRVYDLAGCFGKLKVYLNGER 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 81 DGrevhfcyeggIKAFVEYLN---QNKTPIHPKVFHFTTEQDGIGVEVAMQWNDAYQEGVyCFTNNIPQRDGGTHLvgfr 157
Cdd:PTZ00108 243 IA----------IKSFKDYVDlylPDGEEGKKPPYPFVYTSVNGRWEVVVSLSDGQFQQV-SFVNSICTTKGGTHV---- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 158 TALTRTLNTYMDKEDYSKKAK*SAASGDDVREGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEKLGEFLLENP 237
Cdd:PTZ00108 308 NYILDQLISKLQEKAKKKKKKGKEIKPNQIKNHLWVFVNCLIVNPSFDSQTKETLTTKPSKFGSTCELSEKLIKYVLKSP 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 238 gdakivvnkIIDAARAREAARKARELTRRKGALD---IAGLPgKLADCQEKDPALSE---LYIVEGDSAGGSAKQG---R 308
Cdd:PTZ00108 388 ---------ILENIVEWAQAKLAAELNKKMKAGKksrILGIP-KLDDANDAGGKNSEectLILTEGDSAKALALAGlsvV 457
|
330 340 350
....*....|....*....|....*....|.
gi 1173202403 309 NRKNQAILPLKGKILNVEKARFDKMISSQEV 339
Cdd:PTZ00108 458 GRDYYGVFPLRGKLLNVRDASLKQLMNNKEI 488
|
|
| PLN03128 |
PLN03128 |
DNA topoisomerase 2; Provisional |
37-339 |
1.63e-09 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215593 [Multi-domain] Cd Length: 1135 Bit Score: 59.34 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 37 TEVRFWPSSTIFSDTLFHYDI---LAKRLRELS-FLNSGVSIRLEDERDGrevhfcyeggIKAFVEYLN-----QNKTPI 107
Cdd:PLN03128 188 TKITFKPDLAKFNMTRLDEDVvalMSKRVYDIAgCLGKKLKVELNGKKLP----------VKSFQDYVGlylgpNSREDP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 108 HPKVFHFTTEQDGIGVEVAmqwNDAYQEgvYCFTNNIPQRDGGTHLvgfrTALTRTLNTYMDKEDYSKKAK*SAASGDDV 187
Cdd:PLN03128 258 LPRIYEKVNDRWEVCVSLS---DGSFQQ--VSFVNSIATIKGGTHV----DYVADQIVKHIQEKVKKKNKNATHVKPFQI 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 188 REGLIAVISVKVPDPKFSSQTKDKLVSSEVKTAVEQAMGEklgEFL--LENPGdakiVVNKIIDAARAREAARKARELTR 265
Cdd:PLN03128 329 KNHLWVFVNCLIENPTFDSQTKETLTTRPSSFGSKCELSE---EFLkkVEKCG----VVENILSWAQFKQQKELKKKDGA 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 266 RKGALdiAGLPgKLADCQEKDPALSE---LYIVEGDSAGGSAKQGR---NRKNQAILPLKGKILNVEKARFDKMISSQEV 339
Cdd:PLN03128 402 KRQRL--TGIP-KLDDANDAGGKKSKdctLILTEGDSAKALAMSGLsvvGRDHYGVFPLRGKLLNVREASHKQIMKNAEI 478
|
|
| 39 |
PHA02569 |
DNA topoisomerase II large subunit; Provisional |
140-339 |
3.23e-09 |
|
DNA topoisomerase II large subunit; Provisional
Pssm-ID: 177398 [Multi-domain] Cd Length: 602 Bit Score: 58.23 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 140 FTNNIPQRDGGTHLVGFRTALTRTLNTyMDKEDYSKKAK*SAasgddVREGLIAVISVK-VPDPKFSSQTKDKLVSS--E 216
Cdd:PHA02569 264 FVNGLHTKNGGHHVDCVMDDICEELIP-MIKKKHKIEVTKAR-----VKECLTIVLFVRnMSNPRFDSQTKERLTSPfgE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 217 VKTAVeQAMGEKLGEFLLENPGdakiVVNKIIDAARAREAARKARELTR-RKGALDI-------AGLPGKLADcqekdpa 288
Cdd:PHA02569 338 IRNHI-DLDYKKIAKQILKTEA----IIMPIIEAALARKLAAEKAAETKaAKKAKKAkvakhikANLIGKDAE------- 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1173202403 289 lSELYIVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMISSQEV 339
Cdd:PHA02569 406 -TTLFLTEGDSAIGYLIEVRDEELHGGYPLRGKVLNTWGMSYADILKNKEL 455
|
|
| Toprim |
pfam01751 |
Toprim domain; This is a conserved region from DNA primase. This corresponds to the Toprim ... |
291-335 |
4.78e-07 |
|
Toprim domain; This is a conserved region from DNA primase. This corresponds to the Toprim domain common to DnaG primases, topoisomerases, OLD family nucleases and RecR proteins. Both DnaG motifs IV and V are present in the alignment, the DxD (V) motif may be involved in Mg2+ binding and mutations to the conserved glutamate (IV) completely abolish DnaG type primase activity. DNA primase EC:2.7.7.6 is a nucleotidyltransferase it synthesizes the oligoribonucleotide primers required for DNA replication on the lagging strand of the replication fork; it can also prime the leading stand and has been implicated in cell division. This family also includes the atypical archaeal A subunit from type II DNA topoisomerases. Type II DNA topoisomerases catalyze the relaxation of DNA supercoiling by causing transient double strand breaks.
Pssm-ID: 396354 [Multi-domain] Cd Length: 93 Bit Score: 47.35 E-value: 4.78e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1173202403 291 ELYIVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMIS 335
Cdd:pfam01751 1 ELIIVEGPSDAIALEKALGGGFQAVVAVLGHLLSLEKGPKKKALK 45
|
|
| TOPRIM_TopoIIA |
cd03365 |
TOPRIM_TopoIIA: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the ... |
292-339 |
8.85e-06 |
|
TOPRIM_TopoIIA: topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain of the type found in proteins of the type IIA family of DNA topoisomerases similar to Saccharomyces cerevisiae Topoisomerase II. TopoIIA enzymes cut both strands of the duplex DNA to remove (relax) both positive and negative supercoils in DNA. These enzymes covalently attach to the 5' ends of the cut DNA, separate the free ends of the cleaved strands, pass another region of the duplex through this gap, then rejoin the ends. These proteins also catenate/ decatenate duplex rings. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). This glutamate and two aspartates, cluster together to form a highly acid surface patch. The conserved glutamate may act as a general base in strand joining and as a general acid in strand cleavage by topisomerases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function.
Pssm-ID: 173785 [Multi-domain] Cd Length: 120 Bit Score: 44.21 E-value: 8.85e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1173202403 292 LYIVEGDSAGGSAKQGRN---RKNQAILPLKGKILNVEKARFDKMISSQEV 339
Cdd:cd03365 3 LILTEGDSAKALAVAGLSvvgRDYYGVFPLRGKLLNVREASHKQIMENAEI 53
|
|
| PLN03237 |
PLN03237 |
DNA topoisomerase 2; Provisional |
37-339 |
4.45e-05 |
|
DNA topoisomerase 2; Provisional
Pssm-ID: 215641 [Multi-domain] Cd Length: 1465 Bit Score: 45.24 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 37 TEVRFWPSSTIFSDTLFHYDILA---KRLRELSFlNSGVSIRLEdeRDGREVHfcyeggIKAFVEYLN---QNKTPIHPK 110
Cdd:PLN03237 213 TKVTFKPDLAKFNMTHLEDDVVAlmkKRVVDIAG-CLGKTVKVE--LNGKRIP------VKSFSDYVDlylESANKSRPE 283
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 111 VFHFTTEQDGIGVEVAMQWNDAYQEGVyCFTNNIPQRDGGTHLVGFRTALTRTLNTYMDKEDyskkaK*SAASGDDVREG 190
Cdd:PLN03237 284 NLPRIYEKVNDRWEVCVSLSEGQFQQV-SFVNSIATIKGGTHVDYVTNQIANHVMEAVNKKN-----KNANIKAHNVKNH 357
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173202403 191 LIAVISVKVPDPKFSSQTKDKLvssevkTAVEQAMGEK--LGEFLLEnpgdaKIVVNKIIDAARAREAARKARELTRRKG 268
Cdd:PLN03237 358 LWVFVNALIDNPAFDSQTKETL------TLRQSSFGSKceLSEDFLK-----KVMKSGIVENLLSWADFKQSKELKKTDG 426
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250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1173202403 269 A--LDIAGLPgKLADCQE---KDPALSELYIVEGDSAGGSAKQGRN---RKNQAILPLKGKILNVEKARFDKMISSQEV 339
Cdd:PLN03237 427 AktTRVTGIP-KLEDANEaggKNSEKCTLILTEGDSAKALAVAGLSvvgRNYYGVFPLRGKLLNVREASHKQIMNNAEI 504
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